• Microbiology and Biotechnology Letters
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• v.20 no.6
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• pp.655-662
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• 1992

Pectate lyase produced by recombinant strain containing pectate lyase gene from alkalitolerant Bacillus sp. YA-14 was succesively purified with 257.6 purification folds and a 10.2% yields by the affinity method, eM-cellulose column chromatography followed by gel filtration on Sephadex G-I00 column. The optimal pH and temperature for pectate lyase activity were 10.0 and $60^{\circ}C$, respectively. The enzyme was stable between pH 4.0 and 10.0, and up to $50^{\circ}C$. The molecular weight of this enzyme was estimated to be 43,000 daltons by SDS-PAGE. Amino acid analysis showed that the enzyme contained more polar and basic amino acids, especially serine, glycine and tyrosine, than that of various pectate lyase from other strains. The N-terminal amino acid sequence was Ala-Asp-Leu-Gly-His-Gln-Thr.